Modification of a polypeptide by the process of phosphorylation is an important cellular control mechanism (Greengard, P., Science, 199, 146-152 (1978)) and Krebs, E. G. and Beavo, J. A., Ann. Rev. Biochem., 48, 923-959 (1979)). The protein kinases which modulate the activity of phosphopeptides act as mediators for effector molecules such as cyclic nucleotides or non-cyclic nucleotides, and are termed cyclic nucleotide-dependent or cyclic nucleotide-independent protein kinases. While a great deal is known about the structure, mechanism of activation, and in certain cases the biological function of cyclic AMP- and cyclic GMP-dependent protein kinases (Sharma, R. K., Progress in Nucleic Acid Research and Molecular Biology, (Cohn, W. E., ed.) Vol. 27, pp. 233-288, Academic Press, New York (1982)), it is only recently that the importance of cyclic nucleotide-independent protein kinases in cellular regulation has begun to be appreciated. A variety of enzymes such as phosphorylase kinase (Cohen, P., Burchell, A., Foulkes, J. G., Cohen, P. T. W., Vanaman, T. C., and Nairn, A. C., FEBS Lett., 92, 287-293 (1978) and Depaoli-Roach, A. S., Roach, P. J., and Larner, J., J. Biol. Chem., 254, 4212-4219 (1979)), myosin light chain kinase (Dabrowska, R., Sherry, J. M. F., Aromatorio, D. K., and Hartshorne, D. J., Biochemistry, 17, 253-258 (1978); Yagi, K., Yazawa, M., Kakiuchi, S., Ohshima, M., and Uenishi, K., J. Biol. Chem., 253, 1338-1340 (1978); Hathaway, D. R., and Adelstein, R. S., Proc. Natl. Acad. Sci. U.S.A., 76, 1652-1657 ( 1979); Walsh, M. P., Vallet, B., Autric, F., and Demaille, J. D., J. Biol. Chem., 254, 12,136-12,144 (1979); and Adelstein, R. S., and Klee, C. B., J. Biol. Chem., 256, 7501-7509 (1981)) and glycogen synthase kinase (Payne, M. E., and Soderling, T. R., J. Biol. Chem., 255, 8054-8056 (1980)) are now known to be regulated by calcium-calmodulin, and therefore are termed calcium-calmodulin-dependent protein kinases. A new species of protein kinase, termed C-kinase, which is calmodulin-independent, but calcium-phospholipid-dependent, has also been reported (Takai, Y., Kishimoto, A., Iwasa, Y., Kawahara, Y., Mori, T., and Nishizuka, Y., J. Biol. Chem., 254, 2692-3695 (1979) and Wise, B. C., Raynor, R. L., and Kuo, J. F., J. Biol. Chem., 257, 8481-8488 (1982)). In addition to these protein kinases which regulate the activity of three recognized general mediators of hormone action, cyclic AMP, cyclic GMP, and calcium, other protein kinases specifically regulating the activity of more specialized molecules such as hemin, double-stranded RNA and epidermal growth factor have also been characterized and are named as hemin-controlled repressor (Farrell, P. J., Balkow, K., Hunt, T., Jackson, R. J., and Traschel, H., Cell, 11, 187-200 (1977); Gross, M., Rabinovitz, M., Biochem. Biophys, Res. Commun., 50, 832-838 (1973); Ranu, R. S., and London, I. M., Proc. Natl. Acad. Sci. U.S.A., 73, 4349-4353 (1976); Trachsel, H., Ranu, R. S., and London, I. M., Proc. Natl. Acad. Sci. U.S.A., 75, 3654-3658 (1978); and Tahara, S. M., Traugh, J. A., Sharp, S. B., Lundak, T. S., Safer, B., and Merrick, W. C., Proc. Natl. Acad. Sci. U.S.A., 75, 789-793 (1978 )), dsRNA-activated inhibitor (Farrel et al., supra; Levin, D. H., and London, J. M., Proc. Natl. Acad. Sci. U.S.A., 75, 1121-1125 (1978), and Lenz, J. R., and Baglioni, C., J. Biol. Chem., 253, 4219-4233 (1978)), and epidermal growth factor receptor protein kinase (Ushiro, H., and Cohen, S., J. Biol. Chem., 255, 8363-8365 (1980) and Carpenter, G., King., L., and Cohen, S., J. Biol. Chem., 254, 4884-4891 (1979)), respectively. Other tyrosine protein kinases, that apparently regulate the activity of various RNA tumor viruses, also have been characterized (Witte, O. N., Dasgupta, A., and Baltimore, D., Nature (London), 283, 826-831 (1980); Eckhart, W., Hutchinson, M. A., and Hunter, T., Cell, 18, 925-933 (1979); and Beemon, K., Cell, 24, 145-153 (1981)). Further, there are additional protein kinases such as casein kinases I and II, (Hathaway, G. M., and Traugh, J. A., J. Biol. Chem., 254, 762-768 (1979); and Tuazon, P. T., Bingham, E. W., and Traugh, J. A., Eur. J. Biochem., 94, 497-504 (1979)) and protease activated kinases I, (Tahara, S. M., and Traugh, J. A., J. Biol. Chem., 256, 11,558-11,564, (1981)) and II (Tuazon, P. T., Merrick, W. C., and Traugh, J. A., J. Biol. Chem., 255, 10,954-10,958 (1980)), whose primary regulators and biological functions are unknown. Similarly, neither the primary regulator of self-phosphorylating histidine protein kinase, SPK 380, nor its biological functions is known (Kuroda, Y., and Sharma, R. K., Arch. Biochem. Biophys., 217, 588-596 (1982)) although the partially purified enzyme phosphorylates the alpha subunit of the eukaryotic initiation factor 2 in vitro (Kuroda, Y., Merrick, W. C., and Sharma, R. K., Arch. Biochem. Biophys., 213, 271-275 (1982)).